CAZyme Information: MGYG000001696_02906

Basic Information

• Species: Enterococcus_A raffinosus
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; Enterococcus_A; Enterococcus_A raffinosus
• CAZyme ID: MGYG000001696_02906
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
437	MGYG000001696_49|CGC1	50777.63	5.4437

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001696	4207346	Isolate	India	Asia

• Gene Location: Start: 19086; End: 20399 Strand: +

Full Sequence      

MMKTIDRCLIAENSATQIVRQSIIQLFTELGYQFRNRPETSLILAIESTLETKISLTSNR
LSGKTPSSLFRGAVRLILQQLMGKSQPQTIQPALEEQILMLDIGRKYYSLAKLKRLIRSL
ALFQFTHLQLHFSENEGFGIESLRHPEICSPSHLSQEEIRELIAYAEKFYLEIIPDIDTP
GHVRQLLTHHPEWCLPKTDGSRETSALDILNPEAVDFIKEIYQEFAELFQESRYFHIGAD
EFVDFDQLDQYPSLTSTALKLGSTASGIEPFIQYVNDLIYYLNGFGFIVRVWNDGFYRND
DQEHIHLTNQCEVSYWTRWNPHMAALETYLIRGYTMINHNDNFLYYVLGEAAGYQYPTYE
KINEHFQLTTFASDQKMKKQNQTKGVALSVWADIPKAKSSHEVLADIFWLQAALSEKVYG
DKNKKDDYQEVFEQWMR

Enzyme Prediction     

No EC number prediction in MGYG000001696_02906.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	99	419	2.3e-60	0.9376854599406528

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	1.12e-68	95	421	1	326	Glycosyl hydrolase family 20 (GH20) catalytic domain of dispersin B (DspB), lacto-N-biosidase (LnbB) and related proteins. Dispersin B is a soluble beta-N-acetylglucosamidase found in bacteria that hydrolyzes the beta-1,6-linkages of PGA (poly-beta-(1,6)-N-acetylglucosamine), a major component of the extracellular polysaccharide matrix. Lacto-N-biosidase hydrolyzes lacto-N-biose (LNB) type I oligosaccharides at the nonreducing terminus to produce lacto-N-biose as part of the GNB/LNB (galacto-N-biose/lacto-N-biose I) degradation pathway. The lacto-N-biosidase from Bifidobacterium bifidum has this GH20 domain, a carbohydrate binding module 32, and a bacterial immunoglobulin-like domain 2, as well as a YSIRK signal peptide and a G5 membrane anchor at the N and C termini, respectively. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.
COG3525	Chb	1.91e-43	99	428	266	622	N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
cd02742	GH20_hexosaminidase	3.96e-40	99	393	4	278	Beta-N-acetylhexosaminidases of glycosyl hydrolase family 20 (GH20) catalyze the removal of beta-1,4-linked N-acetyl-D-hexosamine residues from the non-reducing ends of N-acetyl-beta-D-hexosaminides including N-acetylglucosides and N-acetylgalactosides. These enzymes are broadly distributed in microorganisms, plants and animals, and play roles in various key physiological and pathological processes. These processes include cell structural integrity, energy storage, cellular signaling, fertilization, pathogen defense, viral penetration, the development of carcinomas, inflammatory events and lysosomal storage disorders. The GH20 enzymes include the eukaryotic beta-N-acetylhexosaminidases A and B, the bacterial chitobiases, dispersin B, and lacto-N-biosidase. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by the solvent or the enzyme, but by the substrate itself.
pfam00728	Glyco_hydro_20	1.15e-33	99	345	6	266	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06563	GH20_chitobiase-like	4.95e-29	99	426	6	349	The chitobiase of Serratia marcescens is a beta-N-1,4-acetylhexosaminidase with a glycosyl hydrolase family 20 (GH20) domain that hydrolyzes the beta-1,4-glycosidic linkages in oligomers derived from chitin. Chitin is degraded by a two step process: i) a chitinase hydrolyzes the chitin to oligosaccharides and disaccharides such as di-N-acetyl-D-glucosamine and chitobiose, ii) chitobiase then further degrades these oligomers into monomers. This GH20 domain family includes an N-acetylglucosamidase (GlcNAcase A) from Pseudoalteromonas piscicida and an N-acetylhexosaminidase (SpHex) from Streptomyces plicatus. SpHex lacks the C-terminal PKD (polycystic kidney disease I)-like domain found in the chitobiases. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QXJ60839.1	1.02e-312	2	437	1	436
BCA84655.1	8.35e-154	19	437	18	444
EEV40164.1	7.58e-152	20	435	11	428
QOG32092.1	7.58e-152	20	435	11	428
AYJ44717.1	2.16e-151	20	435	11	428

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4H04_A	2.07e-27	152	421	214	476	Lacto-N-biosidasefrom Bifidobacterium bifidum [Bifidobacterium bifidum JCM 1254],4H04_B Lacto-N-biosidase from Bifidobacterium bifidum [Bifidobacterium bifidum JCM 1254],4JAW_A Crystal Structure of Lacto-N-Biosidase from Bifidobacterium bifidum complexed with LNB-thiazoline [Bifidobacterium bifidum JCM 1254],4JAW_B Crystal Structure of Lacto-N-Biosidase from Bifidobacterium bifidum complexed with LNB-thiazoline [Bifidobacterium bifidum JCM 1254],5BXP_A LNBase in complex with LNB-LOGNAc [Bifidobacterium bifidum JCM 1254],5BXP_B LNBase in complex with LNB-LOGNAc [Bifidobacterium bifidum JCM 1254],5BXR_A LNBase in complex with LNB-NHAcDNJ [Bifidobacterium bifidum JCM 1254],5BXR_B LNBase in complex with LNB-NHAcDNJ [Bifidobacterium bifidum JCM 1254],5BXS_A LNBase in complex with LNB-NHAcCAS [Bifidobacterium bifidum JCM 1254],5BXS_B LNBase in complex with LNB-NHAcCAS [Bifidobacterium bifidum JCM 1254],5BXT_A LNBase in complex with LNB-NHAcAUS [Bifidobacterium bifidum JCM 1254],5BXT_B LNBase in complex with LNB-NHAcAUS [Bifidobacterium bifidum JCM 1254]
1YHT_A	3.96e-25	99	423	21	362	Crystalstructure analysis of Dispersin B [Aggregatibacter actinomycetemcomitans]
4AZ7_A	1.84e-20	95	400	6	346	Differentialinhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH [Streptococcus pneumoniae TIGR4]
2YL6_A	1.85e-20	95	400	6	346	Inhibitionof the pneumococcal virulence factor StrH and molecular insights into N-glycan recognition and hydrolysis [Streptococcus pneumoniae TIGR4],4AZ5_A Differential inhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH [Streptococcus pneumoniae TIGR4]
4AZ6_A	1.86e-20	95	400	8	348	Differentialinhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH [Streptococcus pneumoniae TIGR4]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P49610	3.02e-20	83	400	173	526	Beta-N-acetylhexosaminidase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=strH PE=1 SV=2
P96155	1.51e-16	92	244	258	438	Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
P13723	3.09e-16	100	294	161	358	Beta-hexosaminidase subunit A1 OS=Dictyostelium discoideum OX=44689 GN=hexa1 PE=1 SV=1
B2UPR7	4.02e-14	60	430	194	579	Beta-hexosaminidase Amuc_2136 OS=Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) OX=349741 GN=Amuc_2136 PE=1 SV=1
B2UP57	2.07e-13	74	241	86	279	Beta-hexosaminidase Amuc_2018 OS=Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) OX=349741 GN=Amuc_2018 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000067	0.000004	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001696_02906.